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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
27
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pubmed:dateCreated |
2001-7-3
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pubmed:abstractText |
The rat equilibrative nucleoside transporters rENT1 and rENT2 belong to a family of integral membrane proteins with 11 potential transmembrane segments (TMs) and are distinguished functionally by differences in sensitivity to inhibition by nitrobenzylthioinosine (NBMPR). Structurally, the proteins have a large glycosylated extracellular loop between TMs 1 and 2 and a large cytoplasmic loop between TMs 6 and 7. In the present study, we have generated chimeras between NBMPR-sensitive rENT1 and NBMPR-insensitive rENT2, using splice sites at rENT1 residues 99 (end of TM 2), 171 (between TMs 4 and 5), and 231 (end of TM 6) to identify structural domains of rENT1 responsible for transport inhibition by NBMPR. Transplanting the amino-terminal half of rENT2 into rENT1 rendered rENT1 NBMPR-insensitive. Domain swaps within the amino-terminal halves of rENT1 and rENT2 identified two contiguous regions, TMs 3-4 (rENT1 residues 100-171) and TMs 5-6 (rENT1 residues 172-231), as the major sites of NBMPR interaction. Since NBMPR is a nucleoside analogue and functions as a competitive inhibitor of zero-trans nucleoside influx, TMs 3-6 are likely to form parts of the substrate translocation channel.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrobenzylthioinosine,
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Equilibrative Nucleoside Transport...,
http://linkedlifedata.com/resource/pubmed/chemical/Equilibrative Nucleoside...,
http://linkedlifedata.com/resource/pubmed/chemical/Equilibrative-Nucleoside...,
http://linkedlifedata.com/resource/pubmed/chemical/Purine Nucleosides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Slc29a1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Slc29a2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Thioinosine,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8146-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11434784-Affinity Labels,
pubmed-meshheading:11434784-Animals,
pubmed-meshheading:11434784-Biological Transport,
pubmed-meshheading:11434784-Carrier Proteins,
pubmed-meshheading:11434784-Equilibrative Nucleoside Transport Proteins,
pubmed-meshheading:11434784-Equilibrative Nucleoside Transporter 1,
pubmed-meshheading:11434784-Equilibrative-Nucleoside Transporter 2,
pubmed-meshheading:11434784-Oocytes,
pubmed-meshheading:11434784-Peptide Mapping,
pubmed-meshheading:11434784-Purine Nucleosides,
pubmed-meshheading:11434784-Rats,
pubmed-meshheading:11434784-Recombinant Fusion Proteins,
pubmed-meshheading:11434784-Thioinosine,
pubmed-meshheading:11434784-Uridine,
pubmed-meshheading:11434784-Xenopus
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pubmed:year |
2001
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pubmed:articleTitle |
Equilibrative nucleoside transporters: mapping regions of interaction for the substrate analogue nitrobenzylthioinosine (NBMPR) using rat chimeric proteins.
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pubmed:affiliation |
Membrane Transport Research Group, Departments of Physiology and Oncology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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